Novel B-Cell Epitopes of Non-Neutralizing Antibodies in the Receptor-Binding Domain of the SARS-CoV-2 S-Protein with Different Effects on the Severity of COVID-19

Matveev, Andrey L.; Pyankov, Oleg V.; Khlusevich, Yana A.; Tyazhelkova, Olga V.; Emelyanova, Ljudmila A.; Timofeeva, Anna M.; Shipovalov, Andrey V.; Chechushkov, Anton V.; Zaitseva, Natalia S.; Kudrov, Gleb A.; Yusubalieva, Gaukhar M.; Yussubaliyeva, Saule M.; Zhukova, Oxana A.; Tikunov, Artem Yu.; Baklaushev, Vladimir P.; Sedykh, Sergey E.; Lifshits, Galina I.; Tikunova, Nina V.

doi:10.1134/s000629792309002x

Cited by 3 publications

(3 citation statements)

References 29 publications

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“…The oligopeptides most efficiently recognized by antibodies of immunized humans include QF, YK, FI, PQ, PV, GE, As expected, the monoclonal antibodies did not bind to more than one oligopeptide sequence. The epitope recognized by mAb RS17 is located at the N-terminal site of the RBD (348-SVYAVNAVNRKRIS-358) [33]. This epitope is not within the range of oligopeptide sequences tested, so it is not surprising that no positive ELISA signal was observed for this monoclonal antibody.…”

Section: Resultsmentioning

confidence: 99%

Binding of Natural Antibodies Generated after COVID-19 and Vaccination with Individual Peptides Corresponding to the SARS-CoV-2 S-Protein

Timofeeva,

Sedykh,

Litvinova

et al. 2024

Vaccines

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The rapid development of vaccines is a crucial objective in modern biotechnology and molecular pharmacology. In this context, conducting research to expedite the selection of a potent immunogen is imperative. The candidate vaccine should induce the production of antibodies that can recognize the immunogenic epitopes of the target protein, resembling the ones found in recovered patients. One major challenge in vaccine development is the absence of straightforward and reliable techniques to determine the extent to which the spectrum of antibodies produced after vaccination corresponds to antibodies found after recovery. This paper describes a newly developed method to detect antibodies specific to immunogenic epitopes of the target protein in blood plasma and to compare them with antibody spectra generated post vaccination. Comparing the antibody pool generated in the human body after recovering from an infectious disease with the pool formed through vaccination can become a universal method for screening candidate vaccines. This method will enable the identification of candidate vaccines that can induce the production of antibodies similar to those generated in response to a natural infection. Implementing this approach will facilitate the rapid development of new vaccines, even when faced with a pandemic.

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Section: Resultsmentioning

confidence: 99%

Binding of Natural Antibodies Generated after COVID-19 and Vaccination with Individual Peptides Corresponding to the SARS-CoV-2 S-Protein

Timofeeva,

Sedykh,

Litvinova

et al. 2024

Vaccines

View full text Add to dashboard Cite

show abstract

“…The authors proposed that this effect reflected a mechanism of direct steric hinderance, blocking the NAb binding site, or negative cooperativity where a conformational arrangement induced by nNAb binding occluded a neutralisation epitope [80] (Figure 2). Such competition between NAb and nNAb binding may also occur in SARS-CoV-2 infection, and was potentially detected in plasma from COVID-19 patients with severe disease [81].…”

Section: Detrimental Effects Of Nnabs or Nabmentioning

confidence: 99%

Beyond bnAbs: Uses, Risks, and Opportunities for Therapeutic Application of Non-neutralising Antibodies in Viral Infection

Mader,

Dustin

2024

Preprint

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The vast majority of antibodies generated against a virus will be non-neutralising1. However, this does not denote an absence of protective capacity. Yet, within the field there is typically a large focus on antibodies capable of directly blocking infection (neutralising antibodies, nAbs) of either specific viral strains or multiple viral strains (broadly-neutralising antibodies, bnAbs). More recently, a focus on non-neutralising antibodies (nnAbs), or neutralisation-independent effects of nAbs, has emerged. These can have additive effects on protection or in some cases, be a major correlate of protection. As their name suggests, nnAbs do not directly neutralise infection but instead, through their Fc domains, may mediate interaction with other immune effectors to induce clearance of viral particles or virally infected cells. nnAbs may also interrupt viral replication within infected cells. Developing technologies of antibody modification and functionalisation may lead to innovative biologics that harness the activities of nnAbs for antiviral prophylaxis and therapeutics. In this review, we discuss specific examples of nnAb actions in viral infections where they have known importance. We also discuss the potential detrimental effects of such responses. Finally, we explore new technologies for nnAb functionalisation to increase efficacy or introduce favourable characteristics for their therapeutic applications.

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“…The authors proposed that this effect reflected a mechanism of direct steric hindrance, blocking the NAb binding site, or negative cooperativity where a conformational arrangement induced by nNAb binding occluded a neutralisation epitope [ 80 ] ( Figure 2 ). Such competition between NAb and nNAb binding may also occur in SARS-CoV-2 infection and was potentially detected in plasma from COVID-19 patients with severe disease [ 81 ].…”

Section: Detrimental Effects Of Nnabs or Nabmentioning

confidence: 99%

Beyond bNAbs: Uses, Risks, and Opportunities for Therapeutic Application of Non-Neutralising Antibodies in Viral Infection

Mader,

Dustin

2024

Antibodies

View full text Add to dashboard Cite

The vast majority of antibodies generated against a virus will be non-neutralising. However, this does not denote an absence of protective capacity. Yet, within the field, there is typically a large focus on antibodies capable of directly blocking infection (neutralising antibodies, NAbs) of either specific viral strains or multiple viral strains (broadly-neutralising antibodies, bNAbs). More recently, a focus on non-neutralising antibodies (nNAbs), or neutralisation-independent effects of NAbs, has emerged. These can have additive effects on protection or, in some cases, be a major correlate of protection. As their name suggests, nNAbs do not directly neutralise infection but instead, through their Fc domains, may mediate interaction with other immune effectors to induce clearance of viral particles or virally infected cells. nNAbs may also interrupt viral replication within infected cells. Developing technologies of antibody modification and functionalisation may lead to innovative biologics that harness the activities of nNAbs for antiviral prophylaxis and therapeutics. In this review, we discuss specific examples of nNAb actions in viral infections where they have known importance. We also discuss the potential detrimental effects of such responses. Finally, we explore new technologies for nNAb functionalisation to increase efficacy or introduce favourable characteristics for their therapeutic applications.

show abstract

Novel B-Cell Epitopes of Non-Neutralizing Antibodies in the Receptor-Binding Domain of the SARS-CoV-2 S-Protein with Different Effects on the Severity of COVID-19

Cited by 3 publications

References 29 publications

Binding of Natural Antibodies Generated after COVID-19 and Vaccination with Individual Peptides Corresponding to the SARS-CoV-2 S-Protein

Binding of Natural Antibodies Generated after COVID-19 and Vaccination with Individual Peptides Corresponding to the SARS-CoV-2 S-Protein

Beyond bnAbs: Uses, Risks, and Opportunities for Therapeutic Application of Non-neutralising Antibodies in Viral Infection

Beyond bNAbs: Uses, Risks, and Opportunities for Therapeutic Application of Non-Neutralising Antibodies in Viral Infection

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